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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
17
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pubmed:dateCreated |
1977-10-20
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pubmed:abstractText |
Adenylate cyclase in liver membranes was solubilized with Lubrol PX and partially purified by gel filtration. The partially purified enzyme was susceptible to activation by guanyl-5'-yl imidodiphosphate (Gpp(NH)p). Studies on the binding of [3H]Gpp(NH)p to various fractions eluted from the gels revealed that an upper limit of 1% of the Gpp(NH)p binding sites is associated with adenylate cyclase activity stimulated by the nucleotide. The glucagon receptor, pretagged with 125I-glucagon in the membranes, solubilized with Lubrol PX, and fractionated on the same gel columns, eluted in a peak fraction that overlaps with, but is separate from, adenylate cyclase in its Gpp(NH)p-stimulated form. Addition of GTP to the solubilized glucagon-receptor complex caused complete dissociation of the complex, as has been shown with the membrane-bound form of the complex. Since the GTP-sensitive form of the glucagon receptor complex separates from the Gpp(NH)p-sensitive form of adenylate cyclase, it is concluded that the receptor and the enzyme are separate molecules, each associated with a distinct nucleotide regulatory site or component. These findings are discussed in terms of the possible structure of the hormone-sensitive state of adenylate cyclase.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenylate Cyclase,
http://linkedlifedata.com/resource/pubmed/chemical/Glucagon,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Drug
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
252
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5947-50
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:197078-Adenylate Cyclase,
pubmed-meshheading:197078-Animals,
pubmed-meshheading:197078-Cell Membrane,
pubmed-meshheading:197078-Enzyme Activation,
pubmed-meshheading:197078-Glucagon,
pubmed-meshheading:197078-Guanosine Triphosphate,
pubmed-meshheading:197078-Liver,
pubmed-meshheading:197078-Rats,
pubmed-meshheading:197078-Receptors, Cell Surface,
pubmed-meshheading:197078-Receptors, Drug,
pubmed-meshheading:197078-Solubility
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pubmed:year |
1977
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pubmed:articleTitle |
Solubilization and separation of the glucagon receptor and adenylate cyclase in guanine nucleotide-sensitive states.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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